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Conserved domains on  [gi|332661565|gb|AEE86965|]
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PLC-like phosphodiesterases superfamily protein [Arabidopsis thaliana]

Protein Classification

phosphatidylinositol-specific phospholipase C domain-containing protein( domain architecture ID 10171268)

phosphatidylinositol-specific phospholipase C (PI-PLC) domain-containing protein similar to PI-PLC that hydrolyzes a membrane-associated phospholipid, phosphatidylinositol-4,5-bisphosphate, to produce inositol-1,4,5-trisphosphate and diacylglycerol

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0005509
PubMed:  9838022

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 33-313 0e+00

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants; The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, plant PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


:

Pssm-ID: 176556  Cd Length: 285  Bit Score: 530.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  33 FPGCDYMPSDRKNWMA----GVGPEKLHINKIVWPGTHDSATNKIGIRFVSRPFAKCQSLSIYNQLVAGTRVLDIRVQED 108
Cdd:cd08619    1 FPGCDFHTDDHKEWMSlsqlKAMDSSLKLRDIVWPGTHDSATNKIGIPKVSRPFARCQSLSIYNQLCSGARVLDIRVQED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 109 RRVCHGILKTYSVDVVLADLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIHQDDHVFSKTVAELLPKRV 188
Cdd:cd08619   81 RRVCHGCLKTYPVDVVLNDIKRFLSETKSEFVILEIRTEYGHEDPPQFDLWLVEQLGDHLIHQDDSVFSKTLAELLPKRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 189 ICVWKPRKSPQPKHGDPLWSAGYLKDNWIDTDLPSTKFESNIKHLSQQQPATSRKFFYRVENTVTPQPDNPIMCVKPVTK 268
Cdd:cd08619  161 ICIWKPRKSPAPAVGSPLWSSAYLKDNWIDTDLPVTKFESNIKNLLEQPPQDSRKYFYRVENTVTPQFDNPILCVKPVTR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332661565 269 RIHCYAKVFIIECVKRGCADKLQIFSTDFIDNEFVDACVGLTFAR 313
Cdd:cd08619  241 RISQYARLFIPEVFKRGLADRLQIFSLDFIDLDFVDACIGLTVAR 285
 
Name Accession Description Interval E-value
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 33-313 0e+00

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants; The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, plant PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176556  Cd Length: 285  Bit Score: 530.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  33 FPGCDYMPSDRKNWMA----GVGPEKLHINKIVWPGTHDSATNKIGIRFVSRPFAKCQSLSIYNQLVAGTRVLDIRVQED 108
Cdd:cd08619    1 FPGCDFHTDDHKEWMSlsqlKAMDSSLKLRDIVWPGTHDSATNKIGIPKVSRPFARCQSLSIYNQLCSGARVLDIRVQED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 109 RRVCHGILKTYSVDVVLADLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIHQDDHVFSKTVAELLPKRV 188
Cdd:cd08619   81 RRVCHGCLKTYPVDVVLNDIKRFLSETKSEFVILEIRTEYGHEDPPQFDLWLVEQLGDHLIHQDDSVFSKTLAELLPKRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 189 ICVWKPRKSPQPKHGDPLWSAGYLKDNWIDTDLPSTKFESNIKHLSQQQPATSRKFFYRVENTVTPQPDNPIMCVKPVTK 268
Cdd:cd08619  161 ICIWKPRKSPAPAVGSPLWSSAYLKDNWIDTDLPVTKFESNIKNLLEQPPQDSRKYFYRVENTVTPQFDNPILCVKPVTR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332661565 269 RIHCYAKVFIIECVKRGCADKLQIFSTDFIDNEFVDACVGLTFAR 313
Cdd:cd08619  241 RISQYARLFIPEVFKRGLADRLQIFSLDFIDLDFVDACIGLTVAR 285
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 53-170 5.37e-05

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 42.65  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565    53 EKLHINKIVWPGTHDSatnKIGIRFVSrpfAKCQSLSIYNQLVAGTRVLDIRVQEDRR----VCHGILKTYSVDV--VLA 126
Cdd:smart00148   1 MDKPLSHYFIPSSHNT---YLTGKQLW---GESSVEGYIQALDAGCRCVELDCWDGPDgepvIYHGHTFTLPIKLseVLE 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 332661565   127 DLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIH 170
Cdd:smart00148  75 AIKDFAFVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYT 118
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 76-162 2.49e-04

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 42.18  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  76 RFVSRPFAKCQSLSIYNQLVAGTRVLDIRV-----QEDRRVCHGILKTYSVDVVLADLKRFLSETES--EIVILEIRTEF 148
Cdd:PTZ00268  76 RGISASWSKCQGMSVRAQLDHGVRYLDLRVatnpeDANRLYISHTQISVPLADVLEDVKAFLNDPSSanEFIVLDFQHLY 155

                         90
                 ....*....|....
gi 332661565 149 GHEDPPEFDKYLVE 162
Cdd:PTZ00268 156 LTDDSDGKGKFFRE 169
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 82-173 8.28e-04

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 39.03  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565   82 FAKCQSLSIYNQLVAGTRVLDIRVQ----EDRRVCHGilKTYSVDV----VLADLKRFLSETESEIVI--LEIrtefgHE 151
Cdd:pfam00388  24 TGESSVEAYIRALLRGCRCVELDCWdgpdGEPVVYHG--YTLTSKIpfrdVLEAIKDYAFVTSPYPVIlsLEN-----HC 96

                          90       100
                  ....*....|....*....|....*
gi 332661565  152 DPPEFDK---YLVEQLGEHLIHQDD 173
Cdd:pfam00388  97 SPEQQKKmaeILKEIFGDMLYTPPL 121
 
Name Accession Description Interval E-value
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 33-313 0e+00

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants; The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, plant PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176556  Cd Length: 285  Bit Score: 530.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  33 FPGCDYMPSDRKNWMA----GVGPEKLHINKIVWPGTHDSATNKIGIRFVSRPFAKCQSLSIYNQLVAGTRVLDIRVQED 108
Cdd:cd08619    1 FPGCDFHTDDHKEWMSlsqlKAMDSSLKLRDIVWPGTHDSATNKIGIPKVSRPFARCQSLSIYNQLCSGARVLDIRVQED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 109 RRVCHGILKTYSVDVVLADLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIHQDDHVFSKTVAELLPKRV 188
Cdd:cd08619   81 RRVCHGCLKTYPVDVVLNDIKRFLSETKSEFVILEIRTEYGHEDPPQFDLWLVEQLGDHLIHQDDSVFSKTLAELLPKRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 189 ICVWKPRKSPQPKHGDPLWSAGYLKDNWIDTDLPSTKFESNIKHLSQQQPATSRKFFYRVENTVTPQPDNPIMCVKPVTK 268
Cdd:cd08619  161 ICIWKPRKSPAPAVGSPLWSSAYLKDNWIDTDLPVTKFESNIKNLLEQPPQDSRKYFYRVENTVTPQFDNPILCVKPVTR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 332661565 269 RIHCYAKVFIIECVKRGCADKLQIFSTDFIDNEFVDACVGLTFAR 313
Cdd:cd08619  241 RISQYARLFIPEVFKRGLADRLQIFSLDFIDLDFVDACIGLTVAR 285
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 54-310 4.71e-63

Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins; This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176529  Cd Length: 288  Bit Score: 201.42  E-value: 4.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  54 KLHINKIVWPGTHDSATNKI---------------GIRFVSRPFAKCQSLSIYNQLVAGTRVLDIRVQ------EDRRVC 112
Cdd:cd08587    6 DLPLRDLVIPGSHDSGMYTIngdspvgpdqpefgkIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRVAykpdseNKLYFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 113 HGILKTYSVDVVLADLKRFLSETESEIVILEIRTEFGHEDP-PEFDKYLVEQLGEHLIHQ----DDHVFSKTVAELLP-- 185
Cdd:cd08587   86 HGLYSGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDKsPEDHEKLVELLEDIFGDKlcprDSDLLDVTLADLWEsg 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 186 KRVICVWKPRKSPQPkhgDPLWSAGYLKDNWIDTDlPSTKFESNIKHLSQQQPATSRkfFYRVENTVTPQPDNPIMCVK- 264
Cdd:cd08587  166 KRVIVFYDDDLASEG---PYLWPSPYIPDPWANTD-DPQKLIDFLENKLKERRRPDK--FFVLQWILTPQASTIVLGLFs 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 332661565 265 PVTKRIHCYAKVFIIECVKRGCA--DKLQIFSTDFIDN-EFVDACVGLT 310
Cdd:cd08587  240 GLLKKLALRANPALLEWLREQLPgqDGPNIILNDFVDLgEFIDLAIALN 288
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 55-309 9.34e-45

Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins; This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 153.40  E-value: 9.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  55 LHINKIVWPGTHDSATNKIGIRF-VSRPFAKCQSLSIYNQLVAGTRVLDIRVQEDR-----RVCHGI--LKTYSVDVVLA 126
Cdd:cd08557    7 LPLSQLSIPGTHNSYAYTIDGNSpIVSKWSKTQDLSITDQLDAGVRYLDLRVAYDPddgdlYVCHGLflLNGQTLEDVLN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 127 DLKRFLSETESEIVILEIRTEFGHEDPPEFDKyLVEQLGEHLIHQDDHVFSK-----TVAELLP-KRVICVwkpRKSPQP 200
Cdd:cd08557   87 EVKDFLDAHPSEVVILDLEHEYGGDNGEDHDE-LDALLRDVLGDPLYRPPVRaggwpTLGELRAgKRVLLF---YFGGDD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 201 KHGDPLWSAGYLKDNWIDtdlPSTKFESNIKHL-SQQQPATSRKFFYRVENTVTPQPDNPIMCVKPVTKRIHCYAKvfII 279
Cdd:cd08557  163 SSGGYDWGSLNIQDPYAN---GTDKLESLKAFLnSALASPRSADFFYVNQASLTPGRITIAVAGSLYTVATRANPA--LY 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 332661565 280 ECVK--RGCADKLQIFSTDFID-NEFVDACVGL 309
Cdd:cd08557  238 EWLKedGSGASGPNIVATDFVDvGDLIDAVIRL 270
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 52-309 1.99e-20

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176555  Cd Length: 290  Bit Score: 89.22  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  52 PEKLH---INKIVWPGTHDSATNKI-------------------GIRFVSR--PFAKCQSLSIYNQLVAGTRVLDIRVQ- 106
Cdd:cd08616    2 PEKLKdkpLTNLAIPGSHDSFTYSIdkqspvspdqsvqnlvkvfPCIFKKIvkKWSKTQSLTITEQLEAGIRYFDLRIAt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 107 ----EDRRVCHGIlktYSVDV--VLADLKRFLSETESEIVILEIR-----TEFGHEdppEFDKYLVEQLGEHLIHQDDHV 175
Cdd:cd08616   82 kpkdNDLYFVHGL---YGILVkeILEEINDFLTEHPKEVVILDFNhfygmTEEDHE---KLLKMIKSIFGKKLCPRDPDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 176 FSKTVAELLPK--RVICVWKPRKSPQPKHgdpLWSAGYLKDNWIDTdlpsTKFESNIKHLSQQQPATSRKFFYRVENTVT 253
Cdd:cd08616  156 LNVTLEYLWEKgyQVIVFYHDPVAKKPPY---LWPSDAIPSPWPNT----TDPKKLIQFLETTLKERRPPGFHVSQGILT 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332661565 254 PQPdNPIMCVKPVTKRIHCYAKVFI-----IECVKRGCADKLQIFSTDFID-NEFVDACVGL 309
Cdd:cd08616  229 PDV-KTILRHLTSGLLKTLTLRALPkllewLRKQEPGSGQGVNIIIADFVDlDEFIDTVIAL 289
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 63-160 1.22e-18

Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins; This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Their catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer.


Pssm-ID: 176528  Cd Length: 279  Bit Score: 83.87  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  63 PGTHDSATNKIGIRfvsrPFAKCQSLSIYNQLVAGTRVLDIRVQEDRR----VCHGILKT-YSVDVVLADLKRFLSETES 137
Cdd:cd08586   16 PGTHDSGALHGGLS----SSVQCQDWSIAEQLNAGIRFLDIRLRLIDNndlaIHHGPFYQgLTFGDVLNECYSFLDANPS 91

                         90       100
                 ....*....|....*....|....
gi 332661565 138 EIVILEIRTEF-GHEDPPEFDKYL 160
Cdd:cd08586   92 ETIIMSLKQEGsGDGNTDSFAEIF 115
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 54-152 4.50e-15

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176558  Cd Length: 300  Bit Score: 74.34  E-value: 4.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  54 KLHINKIVWPGTHDSATNKI--GI--RFVSRPFAKCQSLSIYNQLVAGTRVLDIRVQEDRrvcHGILKTY---------- 119
Cdd:cd08621    6 DRPLRHIVMPGTHDSGMSSLtgGLwpVDGNDSNTQTQGLSIYDQLRAGARYFDIRPVITH---GGELWTGhyngedasaq 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 332661565 120 -----SVDVVLADLKRFLSETESEIVILEIRTEFGHED 152
Cdd:cd08621   83 gangeSLDDILDEVNRFTDENPGELVILNFSHILNTDN 120
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 63-189 2.41e-13

Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C, X domain containing; This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176559  Cd Length: 276  Bit Score: 68.89  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  63 PGTHDSA-------TNKIGIRfvsrPFAKCQSLSIYNQLVAGTRVLDIRVQEDRR------VCHGILKTYSVDVVLADLK 129
Cdd:cd08622   15 PGTHNSAaydtnsnANESLVD----KYLLTQDLDIWTQLVHGIRYLDLRVGYYPDspdnfwINHDLVRIVPLLTVLNDVR 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332661565 130 RFLSETEsEIVILEIRT-----EFGHEDPPEFDKYLVEQLGEHLIHQD-DHVFSKTVAELLP--KRVI 189
Cdd:cd08622   91 NFVQNTG-EIVVLDFHRfpvgfHSHPEVHDELISLLRQELGDLILRRSrNYGWGPTLSEIWArrKRVI 157
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 55-142 2.08e-07

Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs; This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participates in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG).


Pssm-ID: 176530  Cd Length: 270  Bit Score: 51.18  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  55 LHINKIVWPGTHDSATNKIGIRFVSRPfakcQSLSIYNQLVAGTRVL--DIRVQEDR-RVCHG---ILKTYSVDVVLADL 128
Cdd:cd08588   10 RTYDEYTFLTTHNSFANSEDAFFLAPN----QEDDITKQLDDGVRGLmlDIHDANGGlRLCHSvcgLGDGGPLSDVLREV 85

                         90
                 ....*....|....
gi 332661565 129 KRFLSETESEIVIL 142
Cdd:cd08588   86 VDFLDANPNEVVTL 99
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 58-313 2.59e-07

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176557  Cd Length: 281  Bit Score: 51.24  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  58 NKIVWPGTHDSATNKIgirfvsRPFAKCQSLSIYNQLVAGTRVLDIR-----------VQEDRrVC--HGILKTYSVDVV 124
Cdd:cd08620   10 NRFVLPGAHDAGMNGM------TNLSVTQKDNVSTQLALGARYFDFRpgylwpqtrvlVLLND-LYhqHNMIPGQGFDTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 125 LADLKRFLSETESEIVILEIRTE-FGHE--DPPEFDkyLVEQLGEHLIHQDDHV--------FSKTVAELLP--KRVICV 191
Cdd:cd08620   83 LQDVVTFLKANPTEIVVVHITWDgFDNDcaRPSAQE--VVEALAQALASAKVGYvtsgtvsdLAASYAQLRQtgKRLIVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565 192 WKPRKSpqpkhGDPLWSAGYLKDN--WIDTDLPSTKFESNIKH----LSQQQPATSRKFFYRVENTVTPQPDNPIMCVKP 265
Cdd:cd08620  161 FGDADK-----YDSYSDEDYATSDpqPIIDALNKMLAEGQSGYdytvLQLQATASSTKKGLAAAILSGSHAGSPLLATKA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332661565 266 VtkrihCYAKVF--IIECVKRGCADK-LQIFSTDFIDNEFVDACVGLTFAR 313
Cdd:cd08620  236 M-----FDSATLpwLRENVLARLGDDpLVVLMNDFVDNATTDVAIALTKQR 281
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 62-174 9.08e-07

Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast, SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well, which might suggest they have metal-dependent PI-PLC activity.


Pssm-ID: 176532  Cd Length: 267  Bit Score: 49.33  E-value: 9.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  62 WPGTHDSAtNKIGIRFVSRPFAKC-----QSLSIYNQLVAGTRVLDIRVQ---EDRRVCHG-ILKT----YSVDV----V 124
Cdd:cd08590   15 ILGTHNSY-NSRAYGYGNRYHGVRyldpnQELSITDQLDLGARFLELDVHwttGDLRLCHGgDHGYlgvcSSEDRlfedG 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 332661565 125 LADLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIHQDDH 174
Cdd:cd08590   94 LNEIADWLNANPDEVVILYLEDHGDGGKDDELNALLNDAFGDLLYTPSDC 143
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 53-170 5.37e-05

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 42.65  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565    53 EKLHINKIVWPGTHDSatnKIGIRFVSrpfAKCQSLSIYNQLVAGTRVLDIRVQEDRR----VCHGILKTYSVDV--VLA 126
Cdd:smart00148   1 MDKPLSHYFIPSSHNT---YLTGKQLW---GESSVEGYIQALDAGCRCVELDCWDGPDgepvIYHGHTFTLPIKLseVLE 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 332661565   127 DLKRFLSETESEIVILEIRTEFGHEDPPEFDKYLVEQLGEHLIH 170
Cdd:smart00148  75 AIKDFAFVTSPYPVILSLENHCSPDQQAKMAQMFKEIFGDMLYT 118
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 76-162 2.49e-04

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 42.18  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565  76 RFVSRPFAKCQSLSIYNQLVAGTRVLDIRV-----QEDRRVCHGILKTYSVDVVLADLKRFLSETES--EIVILEIRTEF 148
Cdd:PTZ00268  76 RGISASWSKCQGMSVRAQLDHGVRYLDLRVatnpeDANRLYISHTQISVPLADVLEDVKAFLNDPSSanEFIVLDFQHLY 155

                         90
                 ....*....|....
gi 332661565 149 GHEDPPEFDKYLVE 162
Cdd:PTZ00268 156 LTDDSDGKGKFFRE 169
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 82-173 8.28e-04

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 39.03  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332661565   82 FAKCQSLSIYNQLVAGTRVLDIRVQ----EDRRVCHGilKTYSVDV----VLADLKRFLSETESEIVI--LEIrtefgHE 151
Cdd:pfam00388  24 TGESSVEAYIRALLRGCRCVELDCWdgpdGEPVVYHG--YTLTSKIpfrdVLEAIKDYAFVTSPYPVIlsLEN-----HC 96

                          90       100
                  ....*....|....*....|....*
gi 332661565  152 DPPEFDK---YLVEQLGEHLIHQDD 173
Cdd:pfam00388  97 SPEQQKKmaeILKEIFGDMLYTPPL 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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